Why defensins defend us against bacteria? NMR studies telling a story
Defensins are small (3-5kD) cysteine-rich cationic proteins found in both vertebrate and invertebrates. They are important components of innate immunity against microorganisms including bacteria, fungi and enveloped viruses. Human β-defensin (hBD3) C-terminal peptide analog (Y2) has been proven with...
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sg-ntu-dr.10356-1075342020-09-27T20:27:36Z Why defensins defend us against bacteria? NMR studies telling a story Bai, Yang Konstantin Pervushin School of Biological Sciences Defensins are small (3-5kD) cysteine-rich cationic proteins found in both vertebrate and invertebrates. They are important components of innate immunity against microorganisms including bacteria, fungi and enveloped viruses. Human β-defensin (hBD3) C-terminal peptide analog (Y2) has been proven with higher antibiotic effect against bacteria Pseudomonas, while it shows lower cytotoxic effect on mammalian cells comparing to natural hBD3 protein. The other analog C2 is much less effective. In our study, Y2 and C2 structures in aqueous solution, micelles (DPC), and bicelles (DMPC and DHPC) are analyzed and compared. NMR structures show that Y2 peptide undergoes dramatic conformational change upon interacting with lipid membranes. This peptide may penetrate prokaryotic cell membranes by forming a pore in the membrane which allows efflux. Y2 structure analysis and bacterial killing mechanism study will be useful for antibiotic drug design. [5th Award] 2013-02-01T01:21:07Z 2019-12-06T22:33:24Z 2013-02-01T01:21:07Z 2019-12-06T22:33:24Z 2008 2008 Student Research Poster Bai, Y. (2008, March). Why defensins defend us against bacteria? NMR studies telling a story. Presented at Discover URECA @ NTU poster exhibition and competition, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/107534 http://hdl.handle.net/10220/9073 en © 2008 The Author(s). application/pdf |
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Defensins are small (3-5kD) cysteine-rich cationic proteins found in both vertebrate and invertebrates. They are important components of innate immunity against microorganisms including bacteria, fungi and enveloped viruses. Human β-defensin (hBD3) C-terminal peptide analog (Y2) has been proven with higher antibiotic effect against bacteria Pseudomonas, while it shows lower cytotoxic effect on mammalian cells comparing to natural hBD3 protein. The other analog C2 is much less effective. In our study, Y2 and C2 structures in aqueous solution, micelles (DPC), and bicelles (DMPC and DHPC) are analyzed and compared. NMR structures show that Y2 peptide undergoes dramatic conformational change upon interacting with lipid membranes. This peptide may penetrate prokaryotic cell membranes by forming a pore in the membrane which allows efflux. Y2 structure analysis and bacterial killing mechanism study will be useful for antibiotic drug design. [5th Award] |
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Konstantin Pervushin |
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Konstantin Pervushin Bai, Yang |
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Student Research Poster |
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Bai, Yang |
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Bai, Yang Why defensins defend us against bacteria? NMR studies telling a story |
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Bai, Yang |
title |
Why defensins defend us against bacteria? NMR studies telling a story |
title_short |
Why defensins defend us against bacteria? NMR studies telling a story |
title_full |
Why defensins defend us against bacteria? NMR studies telling a story |
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Why defensins defend us against bacteria? NMR studies telling a story |
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Why defensins defend us against bacteria? NMR studies telling a story |
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why defensins defend us against bacteria? nmr studies telling a story |
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2013 |
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https://hdl.handle.net/10356/107534 http://hdl.handle.net/10220/9073 |
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